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Related Concept Videos

Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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Nuclear Protein Sorting

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Coat Assembly and GTPases01:33

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Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach
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Distinct AAA-ATPase p97 complexes function in discrete steps of nuclear assembly.

M Hetzer1, H H Meyer, T C Walther

  • 1European Molecular Biology Laboratory, Meyerhofstrasse 1, D-69117 Heidelberg, Germany.

Nature Cell Biology
|January 10, 2002
PubMed
Summary

The study reveals the crucial roles of the AAA-ATPase p97 in nuclear envelope (NE) assembly. It identifies distinct p97 complexes responsible for forming a closed NE and subsequent NE growth.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Nuclear envelope (NE) assembly is essential for eukaryotic cell function.
  • While the GTPase Ran is known to be involved, the specific membrane fusion machinery remains largely uncharacterized.
  • NE assembly involves chromatin-associated network formation, fusion into a closed structure, and expansion.

Purpose of the Study:

  • To elucidate the molecular mechanisms and machinery involved in nuclear envelope (NE) assembly.
  • To identify the specific roles of the AAA-ATPase p97 and its adaptors in NE formation.
  • To characterize the membrane fusion events critical for NE biogenesis.

Main Methods:

  • Investigated the function of p97, an AAA-ATPase, and its associated proteins (p47, Ufd1, Npl4) in NE assembly.
  • Utilized biochemical and cell biological approaches to dissect the distinct roles of p97 complexes.
  • Focused on the processes of closed NE formation and subsequent NE growth.

Main Results:

  • p97 has two distinct functions in NE assembly, mediated by different protein complexes.
  • The p97-Ufd1-Npl4 complex is essential for the formation of a closed NE.
  • A separate p97-p47 complex drives the subsequent growth and expansion of the NE.

Conclusions:

  • This study provides the first detailed molecular insights into the fusion events governing NE formation.
  • Identified specific AAA-ATPase complexes (p97-Ufd1-Npl4 and p97-p47) as key players in NE biogenesis.
  • Characterized the distinct roles of p97 in both the initial closure and subsequent expansion of the nuclear envelope.